"Bioactive Food Peptides in Health and Disease" highlights recent developments on bioactive food peptides for the promotion of human health and the prevention/management of chronic diseases. The book provides a comprehensive revision of bioactive peptides obtained from both animal and plant food sources. Aspects related to their bioactivity, mechanism of action, and bioavailability are extensively described along the different chapters.

Research on cell-penetrating peptides for the intracellular delivery of por-phyrin compounds has mainly focused on the use of trans-activator of
transcription (TAT)-derived peptides and, to a lesser extent, on proline-rich
peptides and phosphorescent metalloporphyrins. In this article, we describe
a novel phosphorescent oxygen-sensitive probe for intracellular use which
comprises a bactenecin 7 peptide fragment (15–24) conjugated with the
uncharged monofunctional derivative of Pt(II) coproporphyrin I (PEPP0)....

Macrophages at an inflammatory site release massive
amounts of proteolytic enzymes, including lysosomal cys-teine proteases, which colocalizewith their circulating, tight-binding inhibitors (cystatins, kininogens), so modifying the
protease/antiprotease equilibrium in favor of enhanced
proteolysis. We have explored the ability of human cath-epsins B, KandL to participate in the production of kinins,
using kininogens and synthetic peptides that mimic the
insertion sites of bradykinin on human kininogens....

A small amino acid sequence (LWYIK) inside the HIV-1 gp41 ectodomain
membrane proximal region (MPR) is commonly referred to as a choles-terol-binding domain. To further study this unique and peculiar property
we have used fluorescence spectroscopy techniques to unravel the mem-brane interaction properties of three MPR-derived synthetic peptides: the
membrane proximal region peptide-complete (MPRP-C) which corresponds
to the complete MPR;

Several hematopoietic growth factors (HGFs) have achieved widespread clinical
application. In the United States alone, more than US $5 billion per year of the health care
budget is spent on these factors. The first patients were treated with recombinant human
erythropoietin (rHuEPO, epoetin alfa, Epogen®) in 1985 and the first patients received
recombinant methionyl human granulocyte colony-stimulating factor (r-metHuG-CSF,
filgrastim, Neupogen®) or recombinant human granulocyte-macrophage colonystimulating
factor (rHuGM-CSF, sargramostim, Leukine® or Prokine®) in 1986.

Numerous proteins cannot be sufficiently prepared by ordinary recombi-nant DNA techniques because they are unstable or have deleterious effects
on the host cell. One idea to prepare such proteins is to produce them as
protein inclusions. Here we developed a novel system to effectively prepare
proteins by using peptide tags derived from the insecticidal Cry toxin of a
soil bacterium, Bacillus thuringiensis.

a-Conotoxins are small peptides from cone snail venoms that function as
nicotinic acetylcholine receptor (nAChR)-competitive antagonists differenti-ating between nAChR subtypes. Current understanding about the mechan-ism of these selective interactions is based largely on mutational analyses,
which identify amino acids in the toxin and nAChR that determine the
energetics of ligand binding.

Phage display technology is a powerful selection approach to identify
strong and specific binders to a large variety of targets. In this study, we
compared the efficacy of a phage library displaying human heavy chain
complementarity determining region 3 (HCDR3) repertoires with a set of
conventional random peptide libraries for the identification of CXCR4

The bioactive dipeptide derivative anserine (b-alanyl-1-N-methyl-l-histidine)
is absorbed from the human diet in intact form at the intestinal epithelium.
The purpose of this study was to investigate whether anserine is a substrate
of the H
+
⁄peptide cotransporters 1 and 2 (PEPT1 and PEPT2).

In the present study, EA-CATH1 and EA-CATH2 were identified from
a constructed lung cDNA library of donkey (Equus asinus) as members
of cathelicidin-derived antimicrobial peptides, using a nested PCR-based
cloning strategy. Composed of 25 and 26 residues, respectively,
EA-CATH1 and EA-CATH2 are smaller than most other cathelicidins
and have no sequence homology to other cathelicidins identified to date.

The cathelicidin antimicrobial peptide bactenecin is ab-hairpin molecule
with a single disulfide bond and broad antimicrobial activity. The proform
of bactenecin exists as a dimer, however, and it has been proposed that
bactenecin is released as a dimer in vivo, although there has been little
study of the dimeric form of bactenecin.

Penetratin is a 16-residue peptide [RQIKIWFQNRRM
KWKK(43–58)]derived from the Antennapedia homeo-domain, which is used as a vector for cellular internalization
of hydrophilic molecules. In order to unravel themembrane
translocation mechanism, we synthesized new penetratin
variants. The contribution of the positively charged residues
was studied by double substitutions of Lys and/or Arg resi-dues to Ala, while the specific contribution of Trp48 and
Trp56 was studied by individual substitution of these resi-dues to Phe. ...

We have investigated thein vitrorefolding process of human
proinsulin (HPI) and an artificial mini-C derivative of HPI
(porcine insulin precursor, PIP), and found that they have
significantly different disulfide-formation pathways.HPI
and PIP differ in their amino acid sequences due to the
presence of the C-peptide linker found in HPI, therefore
suggesting that the C-peptide linker may be responsible for
the observed difference in folding behaviour.